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Ian Sitarik

Showing results (1-10 of 14) with videos related to

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Biorxiv : the Preprint Server for Biology|April 27, 2026
Detecting misfolded non-covalent lasso entanglements in protein structures, simulation trajectories, and mass spectrometry dataIan Sitarik, Yang Jiang, Hyebin Song, et al.
Biorxiv : the Preprint Server for Biology|April 27, 2026
Native entanglement misfolding contributes to age-associated structural changes across the Saccharomyces cerevisiae proteomeQuyen V Vu, Ian Sitarik, Daniel A Nissley, et al.
The Journal of Physical Chemistry. B|May 3, 2025
Noncovalent Lasso Entanglements are Common in Experimentally Derived Intrinsically Disordered Protein Ensembles and Strongly Influenced by Protein Length and ChargeQuyen V Vu, Ian Sitarik, Mai Suan Li, et al.
Journal of Molecular Biology|July 11, 2025
Properties Governing Native State Entanglements and Relationships to Protein FunctionJustin Petucci, Ian Sitarik, Yang Jiang, et al.
Biorxiv : the Preprint Server for Biology|September 26, 2025
A widespread protein misfolding mechanism is differentially rescued by chaperones based on gene essentialityIan Sitarik, Quyen Vu, Justin Petucci, et al.
Journal of Molecular Biology|January 31, 2024
Non-covalent Lasso Entanglements in Folded Proteins: Prevalence, Functional Implications, and Evolutionary SignificanceViraj Rana, Ian Sitarik, Justin Petucci, et al.
Nature Communications|December 12, 2025
A widespread protein misfolding mechanism is differentially rescued in vitro by chaperones based on gene essentialityIan Sitarik, Quyen V Vu, Justin Petucci, et al.
Science Advances|March 14, 2025
Protein misfolding involving entanglements providesa structural explanation for the origin of stretched-exponential refolding kineticsYang Jiang, Yingzi Xia, Ian Sitarik, et al.
Biorxiv : the Preprint Server for Biology|April 27, 2026
Natively entangled proteins are linked to human disease and pathogenic mutations likely due to a greater misfolding propensityMaria F Anglero Mendez, Ian Sitarik, Quyen V Vu, et al.
Nature Chemistry|December 5, 2022
How synonymous mutations alter enzyme structure and function over long timescalesYang Jiang, Syam Sundar Neti, Ian Sitarik, et al.
Pageof 2

Showing results (1-10 of 14) with videos related to

Sort By:
Pageof 2
Biorxiv : the Preprint Server for Biology|April 27, 2026
Detecting misfolded non-covalent lasso entanglements in protein structures, simulation trajectories, and mass spectrometry dataIan Sitarik, Yang Jiang, Hyebin Song, et al.
Biorxiv : the Preprint Server for Biology|April 27, 2026
Native entanglement misfolding contributes to age-associated structural changes across the Saccharomyces cerevisiae proteomeQuyen V Vu, Ian Sitarik, Daniel A Nissley, et al.
The Journal of Physical Chemistry. B|May 3, 2025
Noncovalent Lasso Entanglements are Common in Experimentally Derived Intrinsically Disordered Protein Ensembles and Strongly Influenced by Protein Length and ChargeQuyen V Vu, Ian Sitarik, Mai Suan Li, et al.
Journal of Molecular Biology|July 11, 2025
Properties Governing Native State Entanglements and Relationships to Protein FunctionJustin Petucci, Ian Sitarik, Yang Jiang, et al.
Biorxiv : the Preprint Server for Biology|September 26, 2025
A widespread protein misfolding mechanism is differentially rescued by chaperones based on gene essentialityIan Sitarik, Quyen Vu, Justin Petucci, et al.
Journal of Molecular Biology|January 31, 2024
Non-covalent Lasso Entanglements in Folded Proteins: Prevalence, Functional Implications, and Evolutionary SignificanceViraj Rana, Ian Sitarik, Justin Petucci, et al.
Nature Communications|December 12, 2025
A widespread protein misfolding mechanism is differentially rescued in vitro by chaperones based on gene essentialityIan Sitarik, Quyen V Vu, Justin Petucci, et al.
Science Advances|March 14, 2025
Protein misfolding involving entanglements providesa structural explanation for the origin of stretched-exponential refolding kineticsYang Jiang, Yingzi Xia, Ian Sitarik, et al.
Biorxiv : the Preprint Server for Biology|April 27, 2026
Natively entangled proteins are linked to human disease and pathogenic mutations likely due to a greater misfolding propensityMaria F Anglero Mendez, Ian Sitarik, Quyen V Vu, et al.
Nature Chemistry|December 5, 2022
How synonymous mutations alter enzyme structure and function over long timescalesYang Jiang, Syam Sundar Neti, Ian Sitarik, et al.
Pageof 2